Search Results
Overview
| Uniprot ID | A6NHR9 |
|---|---|
| Protein Name | Structural maintenance of chromosomes flexible hinge domain-containing protein 1 |
| Gene Name | SMCHD1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1966 | LGMTPIRKCNDSLRH |
| 1987 | TDCPVPPKRMRREAT |
| 2002 | RQNRIITKTDV**** |
Function
Non-canonical member of the structural maintenance of chromosomes (SMC) protein family that plays a key role in epigenetic silencing by regulating chromatin architecture (By similarity). Promotes heterochromatin formation in both autosomes and chromosome X, probably by mediating the merge of chromatin compartments (By similarity). Plays a key role in chromosome X inactivation in females by promoting the spreading of heterochromatin (PubMed:23542155). Recruited to inactivated chromosome X by Xist RNA and acts by mediating the merge of chromatin compartments: promotes random chromatin interactions that span the boundaries of existing structures, leading to create a compartment-less architecture typical of inactivated chromosome X (By similarity). Required to facilitate Xist RNA spreading (By similarity). Also required for silencing of a subset of clustered autosomal loci in somatic cells, such as the DUX4 locus (PubMed:23143600). Has ATPase activity; may participate in structural manipulation of chromatin in an ATP-dependent manner as part of its role in gene expression regulation (PubMed:29748383). Also plays a role in DNA repair: localizes to sites of DNA double-strand breaks in response to DNA damage to promote the repair of DNA double-strand breaks (PubMed:24790221, PubMed:25294876). Acts by promoting non-homologous end joining (NHEJ) and inhibiting homologous recombination (HR) repair (PubMed:25294876)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0001740 | Barr body |
| Cellular Component | GO:0016604 | nuclear body |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0035861 | site of double-strand break |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Biological Process | GO:0051276 | chromosome organization |
| Biological Process | GO:0009048 | dosage compensation by inactivation of X chromosome |
| Biological Process | GO:0006302 | double-strand break repair |
| Biological Process | GO:2000042 | negative regulation of double-strand break repair via homologous recombination |
| Biological Process | GO:0043584 | nose development |
| Biological Process | GO:0045739 | positive regulation of DNA repair |
| Biological Process | GO:2001034 | positive regulation of double-strand break repair via nonhomologous end joining |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.